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. 1983 Jan 1;209(1):273–276. doi: 10.1042/bj2090273

The Wrb antigen, a receptor for Plasmodium falciparum malaria, is located on a helical region of the major membrane sialoglycoprotein of human red blood cells.

K Ridgwell, M J Tanner, D J Anstee
PMCID: PMC1154085  PMID: 6342608

Abstract

1. Immunoprecipitation of periodate/NaB3H4-labelled human erythrocytes using anti-Wrightb (Wrb) monoclonal antibodies showed that these antibodies specifically react with the major erythrocyte sialoglycoprotein alpha (glycophorin A). 2. Similar experiments on erythrocytes from the only known individual lacking the Wrb antigen but with otherwise normal sialoglycoproteins did not result in the immunoprecipitation of any sialoglycoprotein. 3. We suggest that the Wrb antigen is located on an alpha-helical region between residues 55 and 70 of sialoglycoprotein alpha.

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Selected References

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  1. Adams J., Broviac M., Brooks W., Johnson N. R., Issitt P. D. An antibody, in the serum of a Wr(a+) individual, reacting with an antigen of very high frequency. Transfusion. 1971 Sep-Oct;11(5):290–291. doi: 10.1111/j.1537-2995.1971.tb04416.x. [DOI] [PubMed] [Google Scholar]
  2. Anstee D. J., Edwards P. A. Monoclonal antibodies to human erythrocytes. Eur J Immunol. 1982 Mar;12(3):228–232. doi: 10.1002/eji.1830120311. [DOI] [PubMed] [Google Scholar]
  3. Anstee D. J., Mawby W. J., Parsons S. F., Tanner M. J., Giles C. M. A novel hybrid sialoglycoprotein in Sta positive human erythrocytes. J Immunogenet. 1982 Feb;9(1):51–55. doi: 10.1111/j.1744-313x.1982.tb00782.x. [DOI] [PubMed] [Google Scholar]
  4. Anstee D. J., Mawby W. J., Tanner M. J. Abnormal blood-group-Ss-active sialoglycoproteins in the membrane of Miltenberger class III, IV and V human erythrocytes. Biochem J. 1979 Nov 1;183(2):193–203. doi: 10.1042/bj1830193. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Anstee D. J. The blood group MNSs-active sialoglycoproteins. Semin Hematol. 1981 Jan;18(1):13–31. [PubMed] [Google Scholar]
  6. Chamberlain J. P. Fluorographic detection of radioactivity in polyacrylamide gels with the water-soluble fluor, sodium salicylate. Anal Biochem. 1979 Sep 15;98(1):132–135. doi: 10.1016/0003-2697(79)90716-4. [DOI] [PubMed] [Google Scholar]
  7. Edwards P. A. Monoclonal antibodies that bind to the human erythrocyte-membrane glycoproteins glycophorin A and Band 3 [proceedings]. Biochem Soc Trans. 1980 Jun;8(3):334–335. doi: 10.1042/bst0080334. [DOI] [PubMed] [Google Scholar]
  8. Gahmberg C. G., Andersson L. C. Selective radioactive labeling of cell surface sialoglycoproteins by periodate-tritiated borohydride. J Biol Chem. 1977 Aug 25;252(16):5888–5894. [PubMed] [Google Scholar]
  9. Hopp T. P., Woods K. R. Prediction of protein antigenic determinants from amino acid sequences. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3824–3828. doi: 10.1073/pnas.78.6.3824. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Issitt P. D., Pavone B. G., Wagstaff W., Goldfinger D. The phenotypes En(a-), Wr(a-b-), and En(a+), Wr(a+b-), and further studies on the Wright and En blood group systems. Transfusion. 1976 Sep-Oct;16(5):396–407. doi: 10.1046/j.1537-2995.1976.16577039293.x. [DOI] [PubMed] [Google Scholar]
  11. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  12. Mason D. W., Williams A. F. The kinetics of antibody binding to membrane antigens in solution and at the cell surface. Biochem J. 1980 Apr 1;187(1):1–20. doi: 10.1042/bj1870001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Moore S., Woodrow C. F., McClelland D. B. Isolation of membrane components associated with human red cell antigens Rh(D), (c), (E) and Fy. Nature. 1982 Feb 11;295(5849):529–531. doi: 10.1038/295529a0. [DOI] [PubMed] [Google Scholar]
  14. Pasvol G., Wainscoat J. S., Weatherall D. J. Erythrocytes deficiency in glycophorin resist invasion by the malarial parasite Plasmodium falciparum. Nature. 1982 May 6;297(5861):64–66. doi: 10.1038/297064a0. [DOI] [PubMed] [Google Scholar]
  15. Perkins M. Inhibitory effects of erythrocyte membrane proteins on the in vitro invasion of the human malarial parasite (Plasmodium falciparum) into its host cell. J Cell Biol. 1981 Sep;90(3):563–567. doi: 10.1083/jcb.90.3.563. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Schulte T. H., Marchesi V. T. Conformation of human erythrocyte glycophorin A and its constituent peptides. Biochemistry. 1979 Jan 23;18(2):275–280. doi: 10.1021/bi00569a006. [DOI] [PubMed] [Google Scholar]
  17. Tanner M. J., Jenkins R. E., Anstee D. J., Clamp J. R. Abnormal carbohydrate composition of the major penetrating membrane protein of En(a-) human erythrocytes. Biochem J. 1976 Jun 1;155(3):701–703. doi: 10.1042/bj1550701. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Tomita M., Furthmayr H., Marchesi V. T. Primary structure of human erythrocyte glycophorin A. Isolation and characterization of peptides and complete amino acid sequence. Biochemistry. 1978 Oct 31;17(22):4756–4770. doi: 10.1021/bi00615a025. [DOI] [PubMed] [Google Scholar]

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